ID A0A397HXN9_9EURO Unreviewed; 551 AA.
AC A0A397HXN9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0000259|Pfam:PF16561};
GN ORFNames=CDV56_109540 {ECO:0000313|EMBL:RHZ67547.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ67547.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ67547.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ67547.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ67547.1}.
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DR EMBL; NKHU02000006; RHZ67547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HXN9; -.
DR STRING; 41047.A0A397HXN9; -.
DR VEuPathDB; FungiDB:CDV56_109540; -.
DR OrthoDB; 2056936at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR PANTHER; PTHR10343:SF81; AMP-ACTIVATED PROTEIN KINASE GLYCOGEN-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT DOMAIN 5..80
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT REGION 96..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 57195 MW; B1C6A5C8FBD2600E CRC64;
MGSYAFRWPY PANEVFVTGS FDDWGKTVKL DRYGDVFKKE VQLPSADEKV HYKFVVDGIW
TTDSSAAEED DGSGNINNVL YPGQLKQASN SSQINGTTMA TVTPDETKDS EKRANAATIS
SAAPGSTSAD LAKAVPLEQR SDVPGTFPET PGQEAETFSV NPIPASGTSG NPISLKPGEK
VPDPSTFTSN TVQSTARTDS AGYTQDPSAA TVLAGESTKA SDFAVPPVSG NMIPESSLPM
GEPSATIQSA APTSTTAALA AAVPLESQRH QANAGGIVDE VPRVVRESIA ESHRDPEAAV
NKEAVEEKKE MENELQRRVS KEESTGSPAP STTAGFAATQ TNGGAPVDEV PEAVKHSIAE
AHKDPEAAAN PEAVEEKKEM EDELQKMVPK EEYAGEPAPT ATAATTETAP RATGVEPESQ
SMSPGTATPQ GPTVTTGVAS AKAPEVSGPG VGPEAGPGAG ARTGQNEGTT TLMPSTIPDK
SAAPSEPQTA ATSTPSQPTT APATTAPQEQ TAATTNGQSK PAGQSNGMKN GFREEKKKKK
SFWSRLKEKL K
//